| 纯度 | >90%SDS-PAGE. |
| 种属 | mouse |
| 靶点 | SELL |
| Uniprot No | P18337 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 190-332aa |
| 氨基酸序列 | QCQYVVQCEPLEAPELGTMDCIHPLGNFSFQSKCAFNCSEGRELLGTAET QCGASGNWSSPEPICQVVQCEPLEAPELGTMDCIHPLGNFSFQSKCAFNC SEGRELLGTAETQCGASGNWSSPEPICQETNRSFSKIKEGDYN |
| 预测分子量 | 20 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
| 稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
| 复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是3篇与SELL(L-Selectin)重组蛋白相关的文献摘要，基于领域内常见研究方向整理：
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1. **标题**: "Expression and functional characterization of recombinant human L-selectin in mammalian cells"
**作者**: Smith A, et al.
**摘要**: 研究利用哺乳动物表达系统成功表达并纯化具有生物活性的重组人L-Selectin蛋白。通过流式细胞术验证其与配体(如GlyCAM-1)的结合能力，证实重组蛋白在体外炎症模型中可抑制白细胞黏附，为靶向治疗炎症性疾病提供工具。
2. **标题**: "Structural insights into L-selectin glycosylation-dependent binding using engineered recombinant variants"
**作者**: Chen L, et al.
**摘要**: 通过基因工程技术构建多种糖基化修饰的SELL重组蛋白变体，结合X射线晶体学分析其与碳水化合物配体的相互作用。发现特定糖链结构显著影响L-Selectin的亲和力，为优化免疫调节药物设计提供结构基础。
3. **标题**: "Development of a high-yield Escherichia coli system for producing soluble L-selectin extracellular domain"
**作者**: Wang Y, et al.
**摘要**: 报道一种基于大肠杆菌的重组L-Selectin胞外域高效可溶性表达策略，通过优化密码子与伴侣蛋白共表达，显著提高蛋白产量。纯化后的蛋白在体外趋化实验中显示调控中性粒细胞迁移的活性，适用于大规模生产研究。
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**备注**：以上文献信息为示例性概括，实际文献需通过PubMed、Web of Science等数据库检索确认。若需具体文章，建议使用关键词“recombinant L-selectin protein expression”或“SELL protein functional study”进行精确搜索。
SELL (L-selectin), also known as CD62L, is a cell adhesion molecule belonging to the selectin family, which plays a critical role in leukocyte trafficking and inflammatory responses. It is a transmembrane glycoprotein expressed on leukocytes, including lymphocytes, neutrophils, and monocytes. Structurally, SELL consists of an N-terminal lectin domain, an epidermal growth factor (EGF)-like domain, multiple complement regulatory protein repeats, a transmembrane region, and a short cytoplasmic tail. Its lectin domain mediates calcium-dependent binding to carbohydrate ligands such as GlyCAM-1. CD34. and MadCAM-1 on endothelial cells, facilitating the initial tethering and rolling of leukocytes along blood vessel walls during inflammation or immune surveillance.
Recombinant SELL protein is engineered to mimic the native protein’s functional properties for research and therapeutic applications. Produced via heterologous expression systems (e.g., mammalian cells like HEK293 or CHO cells), recombinant SELL retains post-translational modifications essential for ligand binding, such as glycosylation. This allows it to be used in vitro or in vivo to study leukocyte-endothelial interactions, immune cell migration, and inflammatory pathways. Researchers employ SELL recombinant protein to investigate diseases involving dysregulated leukocyte adhesion, including autoimmune disorders, chronic inflammation, and cancer metastasis. It is also utilized in drug discovery to screen inhibitors targeting selectin-mediated interactions, which may have therapeutic potential in conditions like rheumatoid arthritis or sepsis.
Moreover, SELL recombinant protein serves as a critical tool in developing diagnostic assays or biomarkers for immune activation. Its standardized production ensures batch-to-batch consistency, overcoming limitations of native protein isolation from biological sources. By enabling precise mechanistic studies, recombinant SELL contributes to advancing immunology and inflammation-related research.
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